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Open data
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Basic information
Entry | Database: PDB / ID: 1sf0 | ||||||
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Title | BACKBONE SOLUTION STRUCTURE OF MIXED ALPHA/BETA PROTEIN PF1061 | ||||||
![]() | hypothetical protein PF1061![]() | ||||||
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Function / homology | ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Prestegard, J.H. / Mayer, K.L. / Valafar, H. / Southeast Collaboratory for Structural Genomics (SECSG) | ||||||
![]() | ![]() Title: Backbone solution structures of proteins using residual dipolar couplings: Application to a novel structural genomics target. Authors: Valafar, H. / Mayer, K.L. / Bougault, C.M. / Leblond, P.D. / Jenney, F.E. / Brereton, P.S. / Adams, M.W. / Prestegard, J.H. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 22.8 KB | Display | ![]() |
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PDB format | ![]() | 11.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | ![]() Mass: 8610.884 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED USING PREDOMINANTLY RESIDUAL DIPOLAR COUPLINGS FROM BACKBONE ATOM PAIRS. IT IS A BACKBONE STRUCTURE MODELED AS AN ALA-GLY-PRO POLYPEPTIDE. |
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Sample preparation
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: RDC DIRECTED FRAGMENT ASSEMBLY / Software ordinal: 1 Details: RDCS WERE USED IN THE INITIAL ASSEMBLY OF FOUR FRAGMENTS. RDCS FROM TWO MEDIA WERE USED TO SET RELATIVE ORIENTATIONS OF THE FRAGMENTS. TRANSLATIONAL RELATIONSHIPS OF FRAGMENTS WERE DICTATED ...Details: RDCS WERE USED IN THE INITIAL ASSEMBLY OF FOUR FRAGMENTS. RDCS FROM TWO MEDIA WERE USED TO SET RELATIVE ORIENTATIONS OF THE FRAGMENTS. TRANSLATIONAL RELATIONSHIPS OF FRAGMENTS WERE DICTATED BY SEQUENCE CONNECTIVITIES AND LONG-RANGE NOES. THE ASSEMBLED STRUCTURE WAS MINIMIZED USING A MOLECULAR FORCE FIELD AND RDC ERROR FUNCTION. A TOTAL OF 486 RESTRAINTS WERE USED: 380 RESIDUAL DIPOLAR COUPLING RESTRAINTS, 85 NOE RESTRAINTS (OF WHICH 64 WERE SEQUENTIAL, 11 SHORT-RANGE AND 10 LONG-RANGE), AND 21 DIHEDRAL RESTRAINTS. ALL SIDECHAIN ATOMS BEYOND CB ARE MISSING. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 1 / Conformers submitted total number: 1 |